| Tag | Content |
|---|
| CPLM ID | CPLM-003930 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Enterobactin synthase component F |
Protein Synonyms/Alias | Enterochelin synthase F; Serine-activating enzyme; Seryl-AMP ligase |
Gene Name | entF |
Gene Synonyms/Alias | b0586; JW0578 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 115 | DLRVDSGKPLVFHQL | acetylation | [1] | | 228 | SADILRLKLEFTDGE | acetylation | [1] | | 611 | SGSTGRPKGVMVGQT | acetylation | [2] | | 861 | GRSDDQLKIRGQRIE | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli. Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z. J Proteome Res. 2013 Feb 1;12(2):844-51. [ PMID: 23294111] |
Functional Description | Activates the carboxylate group of L-serine via ATP- dependent PPi exchange reactions to the aminoacyladenylate, preparing that molecule for the final stages of enterobactin synthesis. Holo-EntF acts as the catalyst for the formation of the three amide and three ester bonds present in the cyclic (2,3- dihydroxybenzoyl)serine trimer enterobactin, using seryladenylate and acyl-holo-EntB (acylated with 2,3-dihydroxybenzoate by EntE). |
Sequence Annotation | DOMAIN 976 1043 Acyl carrier.
REGION 1 301 Elongation/condensation.
REGION 482 887 Adenylation.
REGION 1066 1293 Thioesterase.
MOD_RES 1006 1006 O-(pantetheine 4'-phosphoryl)serine |
Keyword | 3D-structure; ATP-binding; Complete proteome; Direct protein sequencing; Enterobactin biosynthesis; Ligase; Multifunctional enzyme; Nucleotide-binding; Phosphopantetheine; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1293 AA |
Protein Sequence | MSQHLPLVAA QPGIWMAEKL SELPSAWSVA HYVELTGEVD SPLLARAVVA GLAQADTLRM 60
RFTEDNGEVW QWVDDALTFE LPEIIDLRTN IDPHGTAQAL MQADLQQDLR VDSGKPLVFH 120
QLIQVADNRW YWYQRYHHLL VDGFSFPAIT RQIANIYCTW LRGEPTPASP FTPFADVVEE 180
YQQYRESEAW QRDAAFWAEQ RRQLPPPASL SPAPLPGRSA SADILRLKLE FTDGEFRQLA 240
TQLSGVQRTD LALALAALWL GRLCNRMDYA AGFIFMRRLG SAALTATGPV LNVLPLGIHI 300
AAQETLPELA TRLAAQLKKM RRHQRYDAEQ IVRDSGRAAG DEPLFGPVLN IKVFDYQLDI 360
PDVQAQTHTL ATGPVNDLEL ALFPDVHGDL SIEILANKQR YDEPTLIQHA ERLKMLIAQF 420
AADPALLCGD VDIMLPGEYA QLAQLNATQV EIPETTLSAL VAEQAAKTPD APALADARYL 480
FSYREMREQV VALANLLRER GVKPGDSVAV ALPRSVFLTL ALHAIVEAGA AWLPLDTGYP 540
DDRLKMMLED ARPSLLITTD DQLPRFSDVP NLTSLCYNAP LTPQGSAPLQ LSQPHHTAYI 600
IFTSGSTGRP KGVMVGQTAI VNRLLWMQNH YPLTGEDVVA QKTPCSFDVS VWEFFWPFIA 660
GAKLVMAEPE AHRDPLAMQQ FFAEYGVTTT HFVPSMLAAF VASLTPQTAR QSCATLKQVF 720
CSGEALPADL CREWQQLTGA PLHNLYGPTE AAVDVSWYPA FGEELAQVRG SSVPIGYPVW 780
NTGLRILDAM MHPVPPGVAG DLYLTGIQLA QGYLGRPDLT ASRFIADPFA PGERMYRTGD 840
VARWLDNGAV EYLGRSDDQL KIRGQRIELG EIDRVMQALP DVEQAVTHAC VINQAAATGG 900
DARQLVGYLV SQSGLPLDTS ALQAQLRETL PPHMVPVVLL QLPQLPLSAN GKLDRKALPL 960
PELKAQAPGR APKAGSETII AAAFSSLLGC DVQDADADFF ALGGHSLLAM KLAAQLSRQV 1020
ARQVTPGQVM VASTVAKLAT IIDAEEDSTR RMGFETILPL REGNGPTLFC FHPASGFAWQ 1080
FSVLSRYLDP QWSIIGIQSP RPNGPMQTAA NLDEVCEAHL ATLLEQQPHG PYYLLGYSLG 1140
GTLAQGIAAR LRARGEQVAF LGLLDTWPPE TQNWQEKEAN GLDPEVLAEI NREREAFLAA 1200
QQGSTSTELF TTIEGNYADA VRLLTTAHSV PFDGKATLFV AERTLQEGMS PERAWSPWIA 1260
ELDIYRQDCA HVDIISPGTF EKIGPIIRAT LNR 1293 |
Gene Ontology | GO:0005829; C:cytosol; IDA:EcoCyc. GO:0009366; C:enterobactin synthetase complex; IDA:EcoCyc. GO:0005886; C:plasma membrane; IDA:EcoCyc. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro. GO:0016874; F:ligase activity; IEA:UniProtKB-KW. GO:0031177; F:phosphopantetheine binding; IDA:EcoCyc. GO:0016740; F:transferase activity; IEA:UniProtKB-KW. GO:0043041; P:amino acid activation for nonribosomal peptide biosynthetic process; IDA:EcoCyc. GO:0009239; P:enterobactin biosynthetic process; IMP:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |